| Abstract: | Two enkephalin-containing polypeptides of 3600 and 4900 daltons have been isolated from extracts of bovine adrenal medulla, purified to homogeneity, and analyzed by a combination of automated Edman degradation and enzymatic time course hydrolysis. The 4900-dalton polypeptide contains two copies of enkephalin, one an internal [Met]enkephalin sequence, the other a [Leu]enkephalin sequence at the carboxyl terminus. Sequence analysis of the 3600-dalton polypeptide has not been completed, but the polypeptide has been shown to contain a single [Met]enkephalin sequence followed by an -Arg-Phe linkage that forms the carboxyl terminus of the molecule. On the basis of these and other findings, we propose that the above enkephalin-containing polypeptides are intermediates in the biosynthesis of the enkephalins and that they are generated by posttranslational processing from a large multivalent enkephalin precursor molecule, proenkephalin. The term "multivalent" is used to indicate a polypeptide with many identical functional sequences. |
